NDLI: Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme.

Please wait, while we are loading the content...

N, N, N', N'-Tetrabromobenzene-1,3-disulfonamide and poly (N-bromo-N-ethylbenzene-1,3-disulfonamide) as new and efficient catalysts for the synthesis of highly substituted 1,6-dihydropyrazine-2,3-dicarbonitrile derivatives.

Docking of a novel DNA methyltransferase inhibitor identified from high-throughput screening: insights to unveil inhibitors in chemical databases.

A simple route for the synthesis of novel N-alkyl-2-(alkylthio)-1H-imidazole derivatives.

An efficient and expeditious synthesis of novel 2,2-dialkyl-2,3-dihydrobenzofurans from phenols and 2,2-dialkylacetaldehydes.

Synthesis of novel spirooxindolo-pyrrolidines, pyrrolizidines, and pyrrolothiazoles via a regioselective three-component [3+2] cycloaddition and their preliminary antimicrobial evaluation.

Identification of novel Interleukin-2 inhibitors through computational approaches.

Synthesis of novel isoquinolinone and 1,2-dihydroisoquinoline scaffolds via Ugi reaction and ring opening reaction of furans.

One pot three component reaction for the rapid synthesis of pyrrolo[1,2-a]benzimidazoles.

Design of peptide affinity ligands for S-protein: a comparison of combinatorial and de novo design strategies.

Plate-based diversity subset screening: an efficient paradigm for high throughput screening of a large screening file.

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme.

One-pot synthesis of tetrazolo[1,5-a]pyrimidines under solvent-free conditions.

Recent progress in asymmetric Biginelli reaction.

Year: 2013 Volume: 17 Issue: 1

Year: 2012 Volume: 16

Year: 2011 Volume: 15

Year: 2010 Volume: 14

Year: 2009 Volume: 13

Year: 2008 Volume: 12

Year: 2007 Volume: 11

Year: 2005 Volume: 9

Year: 2003 Volume: 7

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dong, Yi-Ning Wang, Ling Gu, Qiong Chen, Haiqin Liu, Xiaoming Song, Yuanda Chen, Wei Hagler, Arnold T. Zhang, Hao Xu, Jun
Description	Author Affiliation: Dong YN ( State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, People's Republic of China.)
Abstract	Lactose intolerance is a serious global health problem. A lactose hydrolysis enzyme, thermostable ß-galactosidase, BgaB (from Geobacillus stearothermophilus) has attracted the attention of industrial biologists because of its potential application in processing lactose-containing products. However, this enzyme experiences galactose product inhibition. Through homology modeling and molecular dynamics (MD) simulation, we have identified the galactose binding sites in the thermostable ß-galactosidase BgaB (BgaB). The binding sites are formed from Glu303, Asn310, Trp311, His354, Arg109, Phe341, Try272, Asn147, Glu148, and H354; these residues are all important for enzyme catalysis. A ligand-receptor binding model has been proposed to guide site-directed BgaB mutagenesis experiments. Based upon the model and the MD simulations, we recommend mutating Arg109, Phe341, Trp311, Asn147, Asn310, Try272, and His354 to reduce galactose product inhibition. In vitro site-directed mutagenesis experiments confirmed our predictions. The success rate for mutagenesis was 66.7 %. The best BgaB mutant, F341T, can hydrolyze lactose completely, and is the most promising enzyme for use by the dairy industry. Thus, our study is a successful example of optimizing enzyme catalytic chemical reaction by computer-guided modifying the catalytic site of a wild-type enzyme.
File Format	HTM / HTML
ISSN	13811991
Issue Number	2
Volume Number	17
e-ISSN	1573501X
Journal	Molecular Diversity
Language	English
Publisher	Springer
Publisher Date	2013-05-01
Publisher Place	Netherlands
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Bacterial Proteins Chemistry Galactose Geobacillus Stearothermophilus Lactose Metabolism Beta-galactosidase Amino Acid Motifs Amino Acids Genetics Catalytic Domain Computer-aided Design Escherichia Coli Enzymology Hydrolysis Kinetics Molecular Dynamics Simulation Molecular Sequence Data Mutagenesis, Site-directed Recombinant Proteins Sequence Alignment Thermodynamics Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Medicine Drug Discovery Molecular Biology Physical and Theoretical Chemistry Information Systems Catalysis Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme

Characterization of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus: Enzymatic activity and active site structure☆

Cloning, purification and characterization of Geobacillus stearothermophilus V uroporphyrinogen-III C-methyltransferase: evaluation of its role in resistance to potassium tellurite in Escherichia coli.

Significance of the conserved Tyr352 and Asp380 residues in the catalytic activity of Bacillus stearothermophilus aminopeptidase II as evaluated by site-directed mutagenesis.

The loop structure of Actinomycete glycoside hydrolase family 5 mannanases governs substrate recognition.

Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification.

Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.

Functional characterization of the galactan utilization system of Geobacillus stearothermophilus.

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme.

Similar Documents

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme

Characterization of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus: Enzymatic activity and active site structure☆

Cloning, purification and characterization of Geobacillus stearothermophilus V uroporphyrinogen-III C-methyltransferase: evaluation of its role in resistance to potassium tellurite in Escherichia coli.

Significance of the conserved Tyr352 and Asp380 residues in the catalytic activity of Bacillus stearothermophilus aminopeptidase II as evaluated by site-directed mutagenesis.

The loop structure of Actinomycete glycoside hydrolase family 5 mannanases governs substrate recognition.

Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification.

Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.

Functional characterization of the galactan utilization system of Geobacillus stearothermophilus.

Optimizing lactose hydrolysis by computer-guided modification of the catalytic site of a wild-type enzyme.